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| <StructureSection load='3zyp' size='340' side='right'caption='[[3zyp]], [[Resolution|resolution]] 1.50Å' scene=''> | | <StructureSection load='3zyp' size='340' side='right'caption='[[3zyp]], [[Resolution|resolution]] 1.50Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[3zyp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_13631 Atcc 13631]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZYP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ZYP FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3zyp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Trichoderma_reesei Trichoderma reesei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZYP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZYP FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5Å</td></tr> |
- | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr> |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3zyp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zyp OCA], [http://pdbe.org/3zyp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3zyp RCSB], [http://www.ebi.ac.uk/pdbsum/3zyp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3zyp ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3zyp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zyp OCA], [https://pdbe.org/3zyp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zyp RCSB], [https://www.ebi.ac.uk/pdbsum/3zyp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zyp ProSAT]</span></td></tr> |
| </table> | | </table> |
| + | == Function == |
| + | [https://www.uniprot.org/uniprot/Q7Z9M9_HYPJE Q7Z9M9_HYPJE] |
| <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Atcc 13631]] | |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Goedegebuur, F]] | + | [[Category: Trichoderma reesei]] |
- | [[Category: Hansson, H]] | + | [[Category: Goedegebuur F]] |
- | [[Category: Jacobson, F]] | + | [[Category: Hansson H]] |
- | [[Category: Karkehabadi, S]] | + | [[Category: Jacobson F]] |
- | [[Category: Mitchinson, C]] | + | [[Category: Karkehabadi S]] |
- | [[Category: Piens, K]] | + | [[Category: Mitchinson C]] |
- | [[Category: Sandgren, M]] | + | [[Category: Piens K]] |
- | [[Category: Stals, I]] | + | [[Category: Sandgren M]] |
- | [[Category: Wallace, L]] | + | [[Category: Stals I]] |
- | [[Category: Beta sandwich jelly roll]]
| + | [[Category: Wallace L]] |
- | [[Category: Calcium-binding]]
| + | |
- | [[Category: Carbohydrate-binding]]
| + | |
- | [[Category: Cbm-containing]]
| + | |
- | [[Category: Metal binding protein]]
| + | |
| Structural highlights
Function
Q7Z9M9_HYPJE
Publication Abstract from PubMed
In an effort to characterise the whole transcriptome of the fungus Hypocrea jecorina, cDNA clones of this fungus were identified that encode for previously unknown proteins that are likely to function in biomass degradation. One of these newly identified proteins, found to be co-regulated with the major H. jecorina cellulases, is a protein that was denoted Cellulose induced protein 1 (Cip1). This protein consists of a glycoside hydrolase family 1 carbohydrate binding module connected via a linker region to a domain with yet unknown function. After cloning and expression of Cip1 in H. jecorina, the protein was purified and biochemically characterised with the aim of determining a potential enzymatic activity for the novel protein. No hydrolytic activity against any of the tested plant cell wall components was found. The proteolytic core domain of Cip1 was then crystallised, and the three-dimensional structure of this was determined to 1.5 A resolution utilising sulphur single-wavelength anomalous dispersion phasing (sulphor-SAD). A calcium ion binding site was identified in a sequence conserved region of Cip1 and is also seen in other proteins with the same general fold as Cip1, such as many carbohydrate binding modules. The presence of this ion was found to have a structural role. The Cip1 structure was analysed and a structural homology search was performed to identify structurally related proteins. The two published structures with highest overall structural similarity to Cip1 found were two poly-lyases: CsGL, a glucuronan lyase from H. jecorina and vAL-1, an alginate lyase from the Chlorella virus. This indicates that Cip1 may be a lyase. However, initial trials did not detect significant lyase activity for Cip1. Cip1 is the first structure to be solved of the 23 currently known Cip1 sequential homologs (with a sequence identity cut-off of 25%), including both bacterial and fungal members.
The Crystal Structure of the Core Domain of a Cellulose Induced Protein (Cip1) from Hypocrea jecorina, at 1.5 A Resolution.,Jacobson F, Karkehabadi S, Hansson H, Goedegebuur F, Wallace L, Mitchinson C, Piens K, Stals I, Sandgren M PLoS One. 2013 Sep 5;8(9):e70562. doi: 10.1371/journal.pone.0070562. PMID:24039705[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Jacobson F, Karkehabadi S, Hansson H, Goedegebuur F, Wallace L, Mitchinson C, Piens K, Stals I, Sandgren M. The Crystal Structure of the Core Domain of a Cellulose Induced Protein (Cip1) from Hypocrea jecorina, at 1.5 A Resolution. PLoS One. 2013 Sep 5;8(9):e70562. doi: 10.1371/journal.pone.0070562. PMID:24039705 doi:10.1371/journal.pone.0070562
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